Flexibility and Function in HIV Protease: Dynamics of the HIV-1 Protease Bound to the Asymmetric Inhibitor Kynostatin 272 (KNI-272)
✍ Scribed by Freedberg, Darón I.; Wang, Yun-Xing; Stahl, Stephen J.; Kaufman, Joshua D.; Wingfield, Paul T.; Kiso, Yoshiaki; Torchia, Dennis A.
- Book ID
- 126407025
- Publisher
- American Chemical Society
- Year
- 1998
- Tongue
- English
- Weight
- 123 KB
- Volume
- 120
- Category
- Article
- ISSN
- 0002-7863
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The bioavailability (BA) of a tripeptide protease inhibitor, KNI-272, which has a strong pharmacological potential for treating human immunodeficiency virus type 1 (HIV-l), has been studied in beagle dogs by administering several oral dosage forms. The tested dosage forms were form 1, plain gelatin